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Database: UniProt
Entry: A0A2C9VW79_MANES
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ID   A0A2C9VW79_MANES        Unreviewed;       891 AA.
AC   A0A2C9VW79;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE            EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN   ORFNames=MANES_05G095600 {ECO:0000313|EMBL:OAY49939.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY49939.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY49939.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY49939.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004955}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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DR   EMBL; CM004391; OAY49939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9VW79; -.
DR   STRING; 3983.A0A2C9VW79; -.
DR   EnsemblPlants; OAY49939; OAY49939; MANES_05G095600.
DR   Gramene; OAY49939; OAY49939; MANES_05G095600.
DR   OrthoDB; 20951at2759; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000091857; Chromosome lg5.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003876; F:AMP deaminase activity; IBA:GO_Central.
DR   GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR   GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd01319; AMPD; 1.
DR   Gene3D; 4.10.800.20; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR006329; AMPD.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01429; AMP_deaminase; 1.
DR   PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR   PANTHER; PTHR11359:SF14; AMP DEAMINASE; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          86..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   891 AA;  101982 MW;  CBE51A3DCE3EED39 CRC64;
     MDSSSSSLHL AMAALVGASL MAISAFYVHK RTVDQVLDRL IELRFGSPRS SKMKSVVTDE
     ENSGEEENVD GEAYVWDGEV AMKRKMRSRS ASRSLDDKSV LRSDRVSSSM PNATLSNDWF
     DEDVKFGQQS SRFSAQGQGE RLNFVPLGLA PLRMSTRDGE NKSVNYSTSV TRMASIGRLN
     TPRSPGGNAF GSEWDSDEEG TEYNEDENIF VNENLDTSAD HINEVDSKVQ SSSLPFLGGT
     TNVINDQNLQ EPIAEVKVGV DMLSRNVDIA LARQVGNEAN TIGPSRSTMH EAANIEEEEV
     RKMIRECLDL RNRYVYREGV APWKLDVGEL GTPRLKSDPF HFEPVPATTH HFRMEDGVVH
     VYASEQDTVD LFPVANATTF FTDMHHILRI ISIGNVRTAC HHRLRFLEEK FRLHLLVNAD
     RESLAQKGAP HRDFYNIRKV DTHVHHSACM NQKHLLRFIK SKLRKEPDEV VIFRDGKYMT
     LKEVFESLDL TGYDLNVDLL DVHADKSTFH RFDKFNLKYN PCGQSRLREI FLKQDNLIQG
     RFLAEVTKEV LSDLEASKYQ MAEYRVSIYG RKQSEWDQLA SWFVNNAIYS ENAVWLIQLP
     RLYNVYKQMG TVKCFQNIIE NVFIPLFEVT VDPSTHPQLH VFLMQVVGLD IVDDESRPER
     RPTKHMPKPA EWTNEFNPAY SYYAYYCYAN LYTLNKLRES KGLPTIKFRP HCGEAGDIDH
     LAAAFLLCHN ISHGINLRKS PVLQYLYYLS QIGLAMSPLS NNSLFLDYHR NPFPMFFQRG
     LNVSLSTDDP LQIHLTREPL VEEYSIAAKV WKLSSCDLCE IARNSVYQSG FSHVAKLHWL
     GSKFLLRGPE GNDIHKTNVP HMRIAFRDET WKEEMQYVYS GRAVFPEEVE F
//
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